Nucleation dynamics in two-dimensional cylindrical Ising models and chemotaxis

C. Bosia, M. Caselle, and D. Corá
Phys. Rev. E 81, 021907 – Published 8 February 2010

Abstract

The aim of our work is to study the effect of geometry variation on nucleation times and to address its role in the context of eukaryotic chemotaxis (i.e., the process which allows cells to identify and follow a gradient of chemical attractant). As a first step in this direction we study the nucleation dynamics of the two-dimensional Ising model defined on a cylindrical lattice whose radius changes as a function of time. Geometry variation is obtained by changing the relative value of the couplings between spins in the compactified (vertical) direction with respect to the horizontal one. This allows us to keep the lattice size unchanged and study in a single simulation the values of the compactification radius which change in time. We show both with theoretical arguments and numerical simulations that squeezing the geometry allows the system to speed up nucleation times even in presence of a very small energy gap between the stable and the metastable states. We then address the implications of our analysis for directional chemotaxis. The initial steps of chemotaxis can be modeled as a nucleation process occurring on the cell membrane as a consequence of the external chemical gradient (which plays the role of energy gap between the stable and metastable phases). In nature most of the cells modify their geometry by extending quasi-one-dimensional protrusions (filopodia) so as to enhance their sensitivity to chemoattractant. Our results show that this geometry variation has indeed the effect of greatly decreasing the time scale of the nucleation process even in presence of very small amounts of chemoattractants.

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  • Received 5 August 2009

DOI:https://doi.org/10.1103/PhysRevE.81.021907

©2010 American Physical Society

Authors & Affiliations

C. Bosia1,2,*, M. Caselle1,2,†, and D. Corá3,2,‡

  • 1Dipartimento di Fisica Teorica, Università di Torino and INFN, via P. Giuria 1, I-10125 Torino, Italy
  • 2Center for Complex Systems in Molecular Biology and Medicine, University of Torino, Via Accademia Albertina 13, I-10100 Torino, Italy
  • 3Systems Biology Lab, Institute for Cancer Research and Treatment (IRCC), School of Medicine, Università di Torino, Str. Prov. 142, Km. 3.95, Candiolo I-1060 Torino, Italy

  • *cbosia@to.infn.it
  • caselle@to.infn.it
  • davide.cora@ircc.it

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Vol. 81, Iss. 2 — February 2010

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